Antigen-43-Mediated Autoaggregation ofEscherichia coli Is Blocked by Fimbriation
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چکیده
منابع مشابه
Antigen-43-mediated autoaggregation of Escherichia coli is blocked by fimbriation.
Antigen 43 (Ag43), the product of the flu gene, is a surface-displayed autotransporter protein of Escherichia coli. Ag43 is responsible for the autoaggregation and flocculation of static liquid cultures of many E. coli strains. The expression of Ag43 has been reported to be phase variable and controlled by the product of the oxyR gene. Type 1 fimbriae are thin adhesive thread-like surface organ...
متن کاملAntigen-43-mediated autoaggregation impairs motility in Escherichia coli.
Functional interaction between bacterial surface-displayed autoaggregation proteins such as antigen 43 (Ag43) of Escherichia coli and motility organelles such as flagella has not previously been described. Here, it has been demonstrated for the first time that Ag43-mediated aggregation can inhibit bacterial motility. Ag43 overexpression produces a dominant aggregation phenotype that overrides m...
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Antigen 43 (Ag43) is a self-recognizing surface adhesin found in most Escherichia coli strains. Due to its excellent cell-to-cell aggregation characteristics, Ag43 expression confers clumping and fluffing of cells and promotes biofilm formation. Ag43 expression is repressed by the cellular redox sensor OxyR. Here we used mutant versions of OxyR that are locked in either the reduced or the oxidi...
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Impact of Various Environmental and Growth Conditions on Antigen 43 Gene Expression and Biofilm Formation by Uropathogenic Echserchia coli
ABSTRACT Background and Objectives: Biofilm is a population of bacteria growing on a surface and enclosed in an exopolysaccharides matrix, which increases resistance to antimicrobial agents and immune response. Uropathogenic Escherichia coli (UPEC) are biofilm-forming bacteria and the most common cause of urinary tract infections (UTIs). This study ev...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1999
ISSN: 1098-5530,0021-9193
DOI: 10.1128/jb.181.16.4834-4841.1999